Disulfide bond isomerization in prokaryotes
- PMID: 18342631
- PMCID: PMC2391271
- DOI: 10.1016/j.bbamcr.2008.02.009
Disulfide bond isomerization in prokaryotes
Abstract
Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.
References
-
- Goldberger RF, Epstein CJ, Anfinsen CB. Purification and properties of a microsomal enzyme system catalyzing the reactivation of reduced ribonuclease and lysozyme. J Biol Chem. 1964;239:1406–10. - PubMed
-
- Anfinsen CB, Haber E. Studies on the reduction and re-formation of protein disulfide bonds. J Biol Chem. 1961;236:1361–3. - PubMed
-
- Bardwell JC, McGovern K, Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 1991;67:581–9. - PubMed
-
- Zapun A, Bardwell JC, Creighton TE. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. 1993;32:5083–92. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
